Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [scRNA-seq high fat diet]

ABSTRACT: A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [scRNA-seq high fat diet]

PROVIDER: PRJNA894997 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR22064630.fastq.gz	Fastqsanger.gz
	SRR22064631.fastq.gz	Fastqsanger.gz
	SRR22064632.fastq.gz	Fastqsanger.gz
	SRR22064633.fastq.gz	Fastqsanger.gz

Items per page:

1 - 4 of 4

Similar Datasets

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [RNA-Seq]

Project description:Cancer cells outgrowing in distant organs of metastasis rewire their metabolism to fuel on the available nutrients. While this is often considered an adaptive pressure limiting metastasis formation, some nutrients available at the metastatic site naturally or through changes in organ physiology may inherently promote metastatic growth. We find that the lung, a frequent site of metastasis, is a lipid-rich environment. Moreover, we observe that pathological conditions such as pre-metastatic niche formation and obesity further increase the availability of the fatty acid palmitate in the lung. We find that targeting palmitate processing inhibits spheroid growth in vitro and metastasis formation in lean and obese mice. Mechanistically, we discover that breast cancer cells use palmitate to synthesize acetyl-CoA in a carnitine palmitoyltransferase 1a (CPT1a)-dependent manner. Lysine acetyltransferase 2a (KAT2a), whose expression is promoted by palmitate availability, relies on the available acetyl-CoA to acetylate the NF-B subunit p65. This favors nuclear location of p65 and activates a pro-metastatic transcriptional program. Accordingly, deletion of KAT2a phenocopies CPT1a silencing in vitro as well as in vivo and patients with breast cancer show co-expression of both proteins in metastases across palmitate-rich metastatic sites. In conclusion, we find that palmitate-rich environments foster metastasis growth by increasing p65 acetylation resulting in elevated NF-B signaling.

2022-06-01 | GSE197134 | GEO

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [ChIP-seq]

2022-06-01 | GSE196991 | GEO

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [scRNA-seq]

2022-06-01 | GSE196992 | GEO

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation

Project description:A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation

| PRJNA808245 | ENA

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [scRNA-seq high fat diet]

Project description:Cancer cells outgrowing in distant organs of metastasis rewire their metabolism to fuel on the available nutrients. While this is often considered an adaptive pressure limiting metastasis formation, some nutrients available at the metastatic site naturally or through changes in organ physiology may inherently promote metastatic growth. We find that the lung, a frequent site of metastasis, is a lipid-rich environment. Moreover, we observe that pathological conditions such as pre-metastatic niche formation and obesity further increase the availability of the fatty acid palmitate in the lung. We find that targeting palmitate processing inhibits spheroid growth in vitro and metastasis formation in lean and obese mice. Mechanistically, we discover that breast cancer cells use palmitate to synthesize acetyl-CoA in a carnitine palmitoyltransferase 1a (CPT1a)-dependent manner. Lysine acetyltransferase 2a (KAT2a), whose expression is promoted by palmitate availability, relies on the available acetyl-CoA to acetylate the NF-κB subunit p65. This favors nuclear location of p65 and activates a pro-metastatic transcriptional program. Accordingly, deletion of KAT2a phenocopies CPT1a silencing in vitro as well as in vivo and patients with breast cancer show co-expression of both proteins in metastases across palmitate-rich metastatic sites. In conclusion, we find that palmitate-rich environments foster metastasis growth by increasing p65 acetylation resulting in elevated NF-κB signaling.

2022-10-28 | GSE216695 | GEO

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [RNA-Seq]

Project description:A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [RNA-Seq]

| PRJNA809027 | ENA

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [ChIP-seq]

Project description:A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [ChIP-seq]

| PRJNA808251 | ENA

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [scRNA-seq]

Project description:A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation [scRNA-seq]

| PRJNA808250 | ENA

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation

Project description:This SuperSeries is composed of the SubSeries listed below.

2022-06-01 | GSE196993 | GEO

A palmitate-rich metastatic niche enables metastasis growth via p65 acetylation resulting in pro-metastatic NF-κB signaling.

Project description:Metabolic rewiring is often considered an adaptive pressure limiting metastasis formation; however, some nutrients available at distant organs may inherently promote metastatic growth. We find that the lung and liver are lipid-rich environments. Moreover, we observe that pre-metastatic niche formation increases palmitate availability only in the lung, whereas a high-fat diet increases it in both organs. In line with this, targeting palmitate processing inhibits breast cancer-derived lung metastasis formation. Mechanistically, breast cancer cells use palmitate to synthesize acetyl-CoA in a carnitine palmitoyltransferase 1a-dependent manner. Concomitantly, lysine acetyltransferase 2a expression is promoted by palmitate, linking the available acetyl-CoA to the acetylation of the nuclear factor-kappaB subunit p65. Deletion of lysine acetyltransferase 2a or carnitine palmitoyltransferase 1a reduces metastasis formation in lean and high-fat diet mice, and lung and liver metastases from patients with breast cancer show coexpression of both proteins. In conclusion, palmitate-rich environments foster metastases growth by increasing p65 acetylation, resulting in a pro-metastatic nuclear factor-kappaB signaling.

| S-EPMC7615234 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data